AbstractUsing affinity chromatography with the extrinsic 33 kDa protein as the immobilised ligand, it was demonstrated that the reaction centre complex of photosystem II, composed of the D1, D2 and cytochrome b-559 polypeptides, can directly interact with the 33 kDa protein. By this approach it was possible to purify the reaction centre from solubilised photosystem II core complexes since neither the 47 kDa nor the 43 kDa protein would bind to the ligand
Photosystem II (PSII) is a large membrane protein complex that catalyzes oxidation of water to molec...
Biochemical techniques now exist to produce the oxygen-evolving complex of photosystem II (PSII) and...
ABSTRACT: The 33 kDa manganese-stabilizing extrinsic protein binds to the lumenal side of photosyste...
AbstractUsing affinity chromatography with the extrinsic 33 kDa protein as the immobilised ligand, i...
AbstractThe function of the extrinsic 23 kDa protein of Photosystem II (PSII) was studied with respe...
The effects of the modification of carboxylate groups on the manganese-stabilizing protein on the bi...
AbstractWe report a procedure for one-step isolation of the PS II reaction center complex from PS II...
AbstractChemical crosslinking with a zero-length crosslinker, 1-ethyl-3-(3-dimethylaminopropyl) carb...
The 33-kDa manganese-stabilizing protein (MSP) of Photosystem II (PS II) maintains the functional st...
AbstractLimited proteolysis of the Mn-stabilizing protein (MSP) from the thermophilic cyanobacterium...
Removal of 23 and 17 kDa water-soluble polypeptides from PS II membranes causes a marked decrease in...
AbstractRemoval of the extrinsic 33 kDa polypeptide increased the accessibility to trypsin of a COOH...
AbstractThe nearest neighbour relationships within the D1/D2/cyt b559 complex (PSIIRC) and the CP47/...
AbstractThe function of the extrinsic 23 kDa protein of Photosystem II (PSII) was studied with respe...
This minireview presents a summary of information available on the secondary and tertiary structure ...
Photosystem II (PSII) is a large membrane protein complex that catalyzes oxidation of water to molec...
Biochemical techniques now exist to produce the oxygen-evolving complex of photosystem II (PSII) and...
ABSTRACT: The 33 kDa manganese-stabilizing extrinsic protein binds to the lumenal side of photosyste...
AbstractUsing affinity chromatography with the extrinsic 33 kDa protein as the immobilised ligand, i...
AbstractThe function of the extrinsic 23 kDa protein of Photosystem II (PSII) was studied with respe...
The effects of the modification of carboxylate groups on the manganese-stabilizing protein on the bi...
AbstractWe report a procedure for one-step isolation of the PS II reaction center complex from PS II...
AbstractChemical crosslinking with a zero-length crosslinker, 1-ethyl-3-(3-dimethylaminopropyl) carb...
The 33-kDa manganese-stabilizing protein (MSP) of Photosystem II (PS II) maintains the functional st...
AbstractLimited proteolysis of the Mn-stabilizing protein (MSP) from the thermophilic cyanobacterium...
Removal of 23 and 17 kDa water-soluble polypeptides from PS II membranes causes a marked decrease in...
AbstractRemoval of the extrinsic 33 kDa polypeptide increased the accessibility to trypsin of a COOH...
AbstractThe nearest neighbour relationships within the D1/D2/cyt b559 complex (PSIIRC) and the CP47/...
AbstractThe function of the extrinsic 23 kDa protein of Photosystem II (PSII) was studied with respe...
This minireview presents a summary of information available on the secondary and tertiary structure ...
Photosystem II (PSII) is a large membrane protein complex that catalyzes oxidation of water to molec...
Biochemical techniques now exist to produce the oxygen-evolving complex of photosystem II (PSII) and...
ABSTRACT: The 33 kDa manganese-stabilizing extrinsic protein binds to the lumenal side of photosyste...